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Vol. 9, Issue 7, 1633-1647, July 1998
Division of Biochemistry, School of Biological Sciences, University
of Manchester, Manchester, M13 9PT, United Kingdom
Specificity of vesicular transport is determined by pair-wise
interaction between receptors (SNAP receptors or SNAREs) associated with a transport vesicle and its target membrane. Two additional factors, N-ethylmaleimide-sensitive fusion protein (NSF)
and soluble NSF attachment protein (SNAP) are ubiquitous components of
vesicular transport pathways. However, the precise role they play is
not known. On the basis that NSF and SNAP can be recruited to preformed SNARE complexes, it has been proposed that NSF- and SNAP-containing complexes are formed after SNARE-dependent docking of transport vesicles. This would enable ATPase-dependent complex disassembly to be
coupled directly to membrane fusion. Alternatively, binding and release
of NSF/SNAP may occur before vesicle docking, and perhaps be involved
in the activation of SNAREs. To gain more information about the point
at which so-called 20S complexes form during the transport vesicle
cycle, we have examined NSF/SNAP/SNARE complex turnover on
clathrin-coated vesicle-derived membranes in situ. This has been
achieved under conditions in which the extent of membrane docking can
be precisely monitored. We demonstrate by UV-dependent cross-linking
experiments, coupled to laser light-scattering analysis of membranes,
that complexes containing NSF, SNAP, and SNAREs will form and
dissociate on the surface of undocked transport vesicles.
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